6LPV

structure of Spermidine hydroxycinnamoyl transferases from Arabidopsis thaliana

Summary for 6LPV

• Entry DOI: 10.2210/pdb6lpv/pdb
• Descriptor: Spermidine hydroxycinnamoyl transferase, COENZYME A, SPERMIDINE, ... (4 entities in total)
• Functional Keywords: key words: bahd transferase, phenolamides, spermidine, putrescine, multisite-acylation, molecular mechanism, sequence similarity network, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 51405.14

Authors

Wang, C.Y.,Zhang, P. (deposition date: 2020-01-12, release date: 2021-01-13, Last modification date: 2023-11-29)

Primary citation

Wang, C.,Li, J.,Ma, M.,Lin, Z.,Hu, W.,Lin, W.,Zhang, P.
Structural and Biochemical Insights Into Two BAHD Acyltransferases ( At SHT and At SDT) Involved in Phenolamide Biosynthesis.
Front Plant Sci, 11:610118-610118, 2020

PubMed Abstract: Phenolamides represent one of the largest classes of plant-specialized secondary metabolites and function in diverse physiological processes, including defense responses and development. The biosynthesis of phenolamides requires the BAHD-family acyltransferases, which transfer acyl-groups from different acyl-donors specifically to amines, the acyl-group acceptors. However, the mechanisms of substrate specificity and multisite-acylation of the BAHD-family acyltransferases remain poorly understood. In this study, we provide a structural and biochemical analysis of SHT and SDT, two representative BAHD-family members that catalyze the multisite acylation of spermidine but show different product profiles. By determining the structures of SHT and SDT and using structure-based mutagenesis, we identified the residues important for substrate recognition in SHT and SDT and hypothesized that the acyl acceptor spermidine might adopt a free-rotating conformation in SHT, which can undergo mono-, di-, or tri-acylation; while the spermidine molecule in SDT might adopt a linear conformation, which only allows mono- or di-acylation to take place. In addition, through sequence similarity network (SSN) and structural modeling analysis, we successfully predicted and verified the functions of two uncharacterized BAHD acyltransferases, OAO95042.1 and NP_190301.2, which use putrescine as the main acyl-acceptor. Our work provides not only an excellent starting point for understanding multisite acylation in BAHD-family enzymes, but also a feasible methodology for predicting possible acyl acceptor specificity of uncharacterized BAHD-family acyltransferases.

PubMed: 33519864
DOI: 10.3389/fpls.2020.610118

Experimental method

X-RAY DIFFRACTION (2.297 Å)